Barra D, Martini F, Angelaccio S, Bossa F, Gavilanes F, Peterson D, Bullis B, Schirch L
Biochem Biophys Res Commun. 1983 Nov 15;116(3):1007-12. doi: 10.1016/s0006-291x(83)80242-3.
The sequence of tryptic and chymotryptic peptides from cytosolic and mitochondrial rabbit liver serine hydroxymethyltransferase are compared to the proposed sequence of a protein coded for by the glyA gene of Escherichia coli. The E. coli glyA gene is believed to code for serine hydroxymethyltransferase. Extensive sequence homology between these peptides were found for the proposed E. coli enzyme in the aminoterminal two-thirds of the molecule. All three proteins have identical sequences from residue 222-231. This sequence is known to contain the lysyl residue which forms a Schiff's base with pyridoxal-P in the two rabbit liver enzymes. These results support the interpretation that the proposed sequence of E. coli serine hydroxymethyltransferase is correct. The data also show that cytosolic and mitochondrial serine hydroxymethyltransferase are homologous proteins.
将兔肝脏胞质和线粒体丝氨酸羟甲基转移酶的胰蛋白酶和胰凝乳蛋白酶肽段序列，与大肠杆菌glyA基因编码的一种蛋白质的推测序列进行了比较。据信大肠杆菌glyA基因编码丝氨酸羟甲基转移酶。在分子氨基末端的三分之二区域，发现这些肽段与推测的大肠杆菌酶之间存在广泛的序列同源性。所有这三种蛋白质在第222至231位残基处具有相同的序列。已知该序列包含在两种兔肝脏酶中与磷酸吡哆醛形成席夫碱的赖氨酰残基。这些结果支持了大肠杆菌丝氨酸羟甲基转移酶的推测序列是正确的这一解释。数据还表明，胞质和线粒体丝氨酸羟甲基转移酶是同源蛋白。
